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UniProtKB - P31723 (MAN12_PENCI)
Protein
Mannosyl-oligosaccharide alpha-1,2-mannosidase
Gene
MSDC
Organism
Penicillium citrinum
Status
Functioni
Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.
1 PublicationMiscellaneous
The enzyme is inactivated by reaction of carbodiimide reagents with Asp-375. Since the antibiotic 1-deoxymannojirimycin (DMM) acts as a competitive inhibitor, and it blocks the reaction with carbodiimides, Asp-375 is established as an active site. High activity in presence of EDTA.1 Publication
Catalytic activityi
- 4 H2O + N4-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 β-D-mannose + N4-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)1 PublicationEC:3.2.1.1131 Publication
- 3 H2O + N4-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 β-D-mannose + N4-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)1 PublicationEC:3.2.1.1131 Publication
Cofactori
Ca2+By similarity
pH dependencei
Optimum pH is 5.0.1 Publication
: protein glycosylation Pathwayi
This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 PublicationView all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 375 | Proton donor1 Publication | 1 | |
Metal bindingi | 501 | CalciumBy similarity | 1 |
GO - Molecular functioni
- calcium ion binding Source: InterPro
- mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB-EC
GO - Biological processi
- carbohydrate metabolic process Source: InterPro
- protein glycosylation Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Ligand | Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.2.1.113, 4608 |
UniPathwayi | UPA00378 |
Protein family/group databases
CAZyi | GH47, Glycoside Hydrolase Family 47 |
CLAEi | MSD47C1_PENCI MSD47C2_PENCI |
Names & Taxonomyi
Protein namesi | Recommended name: Mannosyl-oligosaccharide alpha-1,2-mannosidase (EC:3.2.1.1131 Publication)Alternative name(s): Man(9)-alpha-mannosidase |
Gene namesi | Name:MSDC |
Organismi | Penicillium citrinum |
Taxonomic identifieri | 5077 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Penicillium |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Other locations
- membrane Source: InterPro
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 35 | 1 PublicationAdd BLAST | 35 | |
ChainiPRO_0000012085 | 36 – 511 | Mannosyl-oligosaccharide alpha-1,2-mannosidaseAdd BLAST | 476 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 182 | N-linked (GlcNAc...) asparagineCombined sources1 Publication | 1 | |
Disulfide bondi | 332 ↔ 361 | Combined sources1 Publication | ||
Glycosylationi | 366 | N-linked (GlcNAc...) asparagineCombined sources1 Publication | 1 | |
Glycosylationi | 438 | N-linked (GlcNAc...) asparagineCombined sources1 Publication | 1 |
Keywords - PTMi
Disulfide bond, GlycoproteinPTM databases
iPTMneti | P31723 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P31723 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P31723 |
Family & Domainsi
Sequence similaritiesi
Belongs to the glycosyl hydrolase 47 family.Curated
Keywords - Domaini
SignalFamily and domain databases
Gene3Di | 1.50.10.10, 1 hit |
InterProi | View protein in InterPro IPR012341, 6hp_glycosidase-like_sf IPR001382, Glyco_hydro_47 IPR036026, Seven-hairpin_glycosidases |
Pfami | View protein in Pfam PF01532, Glyco_hydro_47, 1 hit |
PRINTSi | PR00747, GLYHDRLASE47 |
SUPFAMi | SSF48225, SSF48225, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P31723-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRLPVSFPLT VLSLLGSTIA HPYGETEAVL RSEPKSNQAK ADAVKEAFQH
60 70 80 90 100
AWNGYMKYAF PHDELTPVSN GHADSRNGWG ASAVDALSTA VIMGKADVVN
110 120 130 140 150
AILEHVADID FSKTSDTVSL FETTIRYLAG MLSGYDLLQG PAKNLVDNQD
160 170 180 190 200
LIDGLLDQSR NLADVLKFAF DTPSGVPYNN INITSHGNDG ATTNGLAVTG
210 220 230 240 250
TLVLEWTRLS DLTGDEEYAK LSQKAESYLL KPQPSSSEPF PGLVGSSINI
260 270 280 290 300
NDGQFADSRV SWNGGDDSFY EYLIKMYVYD PKRFETYKDR WVLAAESTIK
310 320 330 340 350
HLKSHPKSRP DLTFLSSYSN RNYDLSSQHL TCFDGGSFLL GGTVLDRQDF
360 370 380 390 400
IDFGLELVDG CEATYNSTLT KIGPDSWGWD PKKVPSDQKE FYEKAGFYIS
410 420 430 440 450
SGSYVLRPEV IESFYYAHRV TGKEIYRDWV WNAFVAINST CRTDSGFAAV
460 470 480 490 500
SDVNKANGGS KYDNQESFLF AEVMKYSYLA HSEDAAWQVQ KGGKNTFVYN
510
TEAHPISVAR N
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 407 | R → H AA sequence (PubMed:8452520).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D45839 Genomic DNA Translation: BAA08275.1 |
PIRi | S30362 S58766 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D45839 Genomic DNA Translation: BAA08275.1 |
PIRi | S30362 S58766 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1KKT | X-ray | 2.20 | A/B | 1-511 | [»] | |
1KRE | X-ray | 2.20 | A/B | 1-511 | [»] | |
1KRF | X-ray | 2.20 | A/B | 1-511 | [»] | |
2RI8 | X-ray | 2.16 | A/B | 36-510 | [»] | |
2RI9 | X-ray | 1.95 | A/B | 36-510 | [»] | |
SMRi | P31723 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB03206, Duvoglustat DB02742, Kifunensine |
Protein family/group databases
CAZyi | GH47, Glycoside Hydrolase Family 47 |
CLAEi | MSD47C1_PENCI MSD47C2_PENCI |
PTM databases
iPTMneti | P31723 |
Enzyme and pathway databases
UniPathwayi | UPA00378 |
BRENDAi | 3.2.1.113, 4608 |
Miscellaneous databases
EvolutionaryTracei | P31723 |
Family and domain databases
Gene3Di | 1.50.10.10, 1 hit |
InterProi | View protein in InterPro IPR012341, 6hp_glycosidase-like_sf IPR001382, Glyco_hydro_47 IPR036026, Seven-hairpin_glycosidases |
Pfami | View protein in Pfam PF01532, Glyco_hydro_47, 1 hit |
PRINTSi | PR00747, GLYHDRLASE47 |
SUPFAMi | SSF48225, SSF48225, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MAN12_PENCI | |
Accessioni | P31723Primary (citable) accession number: P31723 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | October 1, 1996 | |
Last modified: | June 2, 2021 | |
This is version 117 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families